ITGB6 Gene: Integrin Subunit Beta 6 - Function, Mutations, and Disease Associations

ITGB6 encodes integrin beta-6, a transmembrane receptor subunit that heterodimerizes with integrin alpha-v to form the αvβ6 integrin. This integrin is predominantly expressed on epithelial cells and binds to extracellular matrix proteins such as fibronectin and tenascin. It plays critical roles in epithelial cell adhesion, migration, wound healing, and activation of latent TGF-β. Dysregulation of ITGB6 is implicated in fibrosis, chronic inflammation, and cancer progression.

Tissue Expression

Cell Line Expression

Hotspot Mutations

Mutation functional classification

• Integrin signaling pathway (KEGG: hsa04510)

• TGF-beta signaling pathway (KEGG: hsa04350)

• Focal adhesion (KEGG: hsa04510)

Integrin beta-6 (UniProt P18564) is a 788-amino acid transmembrane protein with a large extracellular domain, a single transmembrane helix, and a short cytoplasmic tail. It exclusively pairs with integrin alpha-v to form the αvβ6 receptor. The extracellular domain contains von Willebrand factor type A domain and multiple integrin beta-6-specific motifs. The cytoplasmic domain contains an NPXY motif critical for signaling. αvβ6 binds to RGD motifs in fibronectin, tenascin, and latency-associated peptide (LAP) of TGF-β, thereby activating TGF-β. This integrin is not expressed in normal adult epithelium but is induced during wound healing and in pathological states such as fibrosis and cancer.